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Biomedical subjects

M S Kaulenas

Publications and source records attributed to M S Kaulenas.

At least 19 recordsLinked to original sources

Analysis of the translational capacity of the male accessory gland during aging in Acheta domesticus.

The protein synthesizing capacity of the male cricket accessory gland was inspected for changes associated with aging by analysis of organs from young (2 weeks post-imaginal molt), middle-aged (4 and 6 weeks) and senescent (8 weeks) animals. Total RNA content and the percentage of ribosomes in polysomes show an increase up to 4 weeks and then a steady decline. The rates of protein synthesis by young and old glands incubated in vitro were comparable, although the old glands were significantly less efficient in precursor uptake and therefore showed lower incorporation levels. The overall picture appears to be one of a steady but unspectacular decline in protein synthesizing capacity in aging animals. The quality of the secretory proteins formed by young and old glands was inspected by SDS--polyacrylamide gel electrophoresis and by isoelectric focusing, using both wide and narrow pH-range gels. While some differences in the banding patterns of isoelectric focusing gels were detected, they were eliminated by the inclusion of Triton X-100 in the gels. No other evidence for age-associated qualitative or quantitative changes was detected, strongly suggesting that proteins from young and old glands are identical.

Aging↗

Ribosomal proteins in normal simian cells, SV40-transformed simian cells, and simian cells infected with SV40, adenovirus 5, and vesicular stomatitis virus.

The protein patterns of monosomes and polysomes isolated from the T-22 line of SV40-transformed GMK cells and from uninfected CV-1 cells and CV-1 cells infected with SV40, adenovirus 5, or vesicular stomatitis virus were analyzed by two-dimensional PAGE. All gel patterns were similar except for the presence of one additional protein associated with T-22 monosomes.

Adenoviruses, Human↗

Changes in ribosome-associated proteins during sea urchin development.

Ribosomes isolated from unfertilised eggs of the sea urchin, Strongylocentrotus purpuratus, have a higher protein: RNA ratio than ribosomes extracted from blastula stage ribosomes. Approximately 64 additional protein equivalents are found per ribosome. Most of the proteins are of high molecular weight and are tightly bound, being resistant to high-salt and EDTA treatment. The majority of the proteins appear to be basic in nature and remain associated with the 40S subunit on dissociation of the ribosomes. The possible physiological significance of the additional proteins is discussed in terms of the activation of protein synthesis following fertilisation. Sea urchin ribosomes, isolated from various stages of development, showed differential protein-labelling patterns. The high molecular-weight proteins had preferentially higher specific activities and one ribosomal protein was particularly highly labelled, reaching a maximum at the gastrula stage of development. The functional role of this highly labelled protein during development is discussed.

Animals↗

Initiation factor distribution in Xenopus laevis eggs.

The distribution of activity similar to that of one of the initiation factors (IF2) was determined as a function of developmental stage in Xenopus laeviseggs and embryos. In vivo exposure of mature oocytes to hormone increases the total amount of detectable factor activity and facilitates the binding of IF2-like factor to ribosomes. The quality of factor bound is not correlated with polysome content.

Animals↗